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Fast dissociation kinetics between individual E‐cadherin fragments revealed by flow chamber analysis
Author(s) -
Perret Emilie,
Benoliel AnneMarie,
Nassoy Pierre,
Pierres Anne,
Delmas Véronique,
Thiery JeanPaul,
Bongrand Pierre,
Feracci Hélène
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.11.2537
Subject(s) - kinetics , cadherin , biophysics , biology , dissociation (chemistry) , extracellular , microbiology and biotechnology , receptor–ligand kinetics , adhesion , biochemistry , cell , chemistry , physics , receptor , quantum mechanics , organic chemistry
E‐cadherin is the predominant adhesion molecule of epithelia. The interaction between extracellular segments of E‐cadherin in the membrane of opposing cells is homophilic and calcium dependent. Whereas it is widely accepted that the specificity of the adhesive interaction is localized to the N‐terminal domain, the kinetics of the recognition process are unknown. We report the first quantitative data describing the dissociation kinetics of individual E‐cadherin interactions. Aggregation assays indicate that the two outermost domains of E‐cadherin (E/EC1–2) retain biological activity when chemically immobilized on glass beads. Cadherin fragment trans ‐interaction was analysed using a flow chamber technique. Transient tethers had first‐order kinetics, suggesting a unimolecular interaction. The unstressed lifetime of individual E‐cadherin interactions was as brief as 2 s. A fast off rate and the low tensile strength of the E‐cadherin bond may be necessary to support the high selectivity and plasticity of epithelial cell interactions.